Key result
The amino acid sequence of the African swine fever virus attachment protein p12 showed a high degree of conservation among field isolates and no mutations after adaptation to Vero cells.
The African swine fever virus attachment protein p12 is highly conserved across field isolates and tissue culture adaptations, suggesting it is a stable viral component.
p12 conservation in ASFV may guide veterinary diagnostics; leaves open vaccine cross-protection in natural swine hosts.
Comparison of the amino acid sequence of the African swine fever virus attachment protein p12 from different field virus isolates, deduced from the nucleotide sequence of the gene, revealed a high degree of conservation. No mutations were found after adaptation to Vero cells, and a polypeptide with similar characteristics was present in an IBRS2-adapted virus. The sequence of the 5' flanking region was conserved among the isolates, whereas sequences downstream of the gene were highly variable in length and contained direct repeats in tandem that may account for the deletions found in different isolates. Protein p12 was synthesized in swine macrophages infected with all of the viruses tested.
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Angulo et al. (1992) studied African swine fever virus. Sequence comparison of p12 gene was evaluated on Amino acid sequence conservation and mutations. The amino acid sequence of the African swine fever virus attachment protein p12 showed a high degree of conservation among field isolates and no mutations after adaptation to Vero cells.
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